ID A0A3P8VYD7_CYNSE Unreviewed; 1075 AA.
AC A0A3P8VYD7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 6 {ECO:0000313|Ensembl:ENSCSEP00000017395.1};
GN Name=ADAMTS6 {ECO:0000313|Ensembl:ENSCSEP00000017395.1};
OS Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000017395.1, ECO:0000313|Proteomes:UP000265120};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000017395.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|Ensembl:ENSCSEP00000017395.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR AlphaFoldDB; A0A3P8VYD7; -.
DR Ensembl; ENSCSET00000017613.1; ENSCSEP00000017395.1; ENSCSEG00000011127.1.
DR GeneTree; ENSGT00940000156571; -.
DR OMA; HYDGICY; -.
DR Proteomes; UP000265120; Chromosome 14.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 5.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF27; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 6; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 4.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 5.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 4.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR613273-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000265120};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 208..426
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1037..1075
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 177..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 362
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 421
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 284..345
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 320..327
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 339..421
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 378..405
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 448..470
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 459..477
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 465..500
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 490..505
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 528..565
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 532..570
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 543..555
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1075 AA; 120022 MW; 872C49704AFAC2D7 CRC64;
KLLACKLVST AVLLLLWCFF TVWYKEFLSY VQHYQLTVPV RVDENGEFLN SDPPESQLFY
KLSAYGKHFH LNLTLNPHLV SKHFTVEYWG KEGLEWRHNT VDNCHYVGFL QNQHSTTRVA
LSNCRGLHGV ITTEEEQYLI EPLKNISSTT SSQWNLEEAQ QHVIYKMSSG APCQFNTPSP
GHLAHLPPNS SRHSSSTHRQ KRSVSTERFV ETLVVADKMM VGYHGRKDIE HYILSVMNIV
AKLYHDASLG NVVNIIVTRL IVLTEDQPNL EINHHADKSL DSFCKWQKSI LSHHNDGNSI
PENGMAHHDN AVLITRYDIC TYKNKPCGTL GLASVAGMCE PERSCSINED IGLSSAFTIA
HEIGHNFGMN HDGIGNACGT KGHETAKLMA AHITANTNPF SWSACSKDYI TSFLDSGRGT
CLDNEPLKRD FLYPTVAPGQ VYDADEQCRF QYGASSRQCK YGEVCRELWC LSKSNRCVTN
SIPAAEGTLC QTGSIEKGWC YQGECVVFGT WPQSADGGWG PWSMWGECSR TCGGGVSSST
RHCDSPAPSG GGKYCLGERK RYRSCNIDAC PAGSRDFREK QCADFDNMPF RGKYYNWKPY
TGGGVKPCAL NCLAEGYNFY TERSPAVIDG TRCLADSLNI CINGECKHVG CDNILGSDAK
EDRCRVCGGD GSTCEATEGL FNESLPRGGY MDVVQIPKGS VHIEIKELLD FCNYLALKSE
EDDYYINGAW TIDWPRKFDI AGTVFHYKRP SDEPESLEAL GATTENLFVM VLLQEQNMGI
RYKFNVPIQR TGSGDNEVGF SWHHLPWSEC SATCAGGSQE QGVVCKRLDD NSVVQNSYCD
PDSKPPENQR DCNTEPCPPE WFIGDWSECG KTCDGGIRTR TVLCIRKIGR AEEETLEDTH
CLTHRPLERE SCNNQSCPPK WVTLDWSECT PKCGPGYKHR IALCKSSDLS KTFPPAHCPS
HNKPPVRIRC SLGRCPPPRW IPGEWGQCSA QCGLGQQMRT VQCLSYTGQP SHECPESLRP
STMQQCESKC DATPIANGDE CKDVNKVAYC PLVLKFKFCS RGYFRQMCCK TCQGH
//
